rsmG protein (Escherichia coli K12 DH10B) - STRING interaction network
"rsmG" - 16S rRNA methyltransferase GidB in Escherichia coli K12 DH10B
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
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Gene Fusion
rsmG16S rRNA methyltransferase GidB; Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Requires the intact 30S subunit for methylation (207 aa)    
Predicted Functional Partners:
tRNA uridine 5-carboxymethylaminomethyl modification protein GidA; NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34 (629 aa)
tRNA modification GTPase TrmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34 (454 aa)
Bifunctional (p)ppGpp synthetase II/ guanosine-3’,5’-bis pyrophosphate 3’-pyrophosphohydrolase; In eubacteria ppGpp (guanosine 3’-diphosphate 5-’ diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the synthesis and degradation of ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c- di-GMP induces it (704 aa)
Methyltransferase; Catalyzes the 2’-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. In vitro, active on the assembled 30S subunit, but not naked 16S rRNA or 70S ribosomes (286 aa)
GTP-binding protein Era; An essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring on the order of seconds whereas hydrolysis occurs on the order of minutes. Plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing and 30S ribosomal subunit biogenesis. Its presence in the 30S subunit may prevent translation initiation. Seems to be critical for maintaining cell growth and cell divison rates; a dramatic reduction in Era protein levels temporarily arrests cell growth just before cytokinesis (at [...] (301 aa)
DNA topoisomerase IV subunit A; Topoisomerase IV is essential for chromosome segregation; it is the principal protein responsible for decatenating newly replicated chromosomes (PubMed-9334322). It relaxes supercoiled DNA (PubMed-12269820, PuMed-16023670, PubMed-21300644). MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation (PubMed-20921377) (752 aa)
F0F1 ATP synthase subunit B; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (156 aa)
Cell division protein MraZ; Negatively regulates its own expression and that of the subsequent genes in the proximal part of the division and cell wall (dcw) gene cluster. Acts by binding directly to DNA. May also regulate the expression of genes outside the dcw cluster (152 aa)
GTP-binding protein EngA; GTPase that plays an essential role in the late steps of ribosome biogenesis. GTPase point mutations (but not a deletion mutant) are suppressed by mild overexpression of RelA, probably due to increased levels of the stringent response mediator (p)ppGpp. 50S subunits assembled in the absence of Der are defective and unable to assemble into 70S ribosomes. GTPase activity is stimulated by YihI. Overexpression rescues an rrmJ deletion, stabilizing the 70S ribosome. Der and RrmJ are likely to share a mechanism to stabilize 50S ribosomal subunits at a very late stag [...] (490 aa)
Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates (PubMed-24812405). Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed-12226666). Functions as a peptidyl- prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity (432 aa)
Your Current Organism:
Escherichia coli K12 DH10B
NCBI taxonomy Id: 316385
Other names: E. coli str. K-12 substr. DH10B, Escherichia coli DH10B, Escherichia coli K12 DH10B, Escherichia coli str. K-12 substr. DH10B, Escherichia coli str. K12 substr. DH10B, Escherichia coli strain K12 substrain DH10B
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